Human Cathelicidin Protein expressed in Escherichia coli (E. coli) - ABIN2123814
Choi, Kim, Chi, Kwon, Chang: Modulating the internalization of bacille Calmette-Guérin by cathelicidin in bladder cancer cells. in Urology 2015
Treatment of asthma patients with vitamin D reduced respiratory infections, and this effect was related to the increase of cathelicidin LL-37.
Plasma LL-37 and NF-kappaB may play important roles in chronic immune inflammation. Decreased LL-37 levels may be particularly high risk for patients in stage IV COPD.
The human host defence peptide LL-37 is a broad-spectrum antibiotic. Residues 18-29 in LL-37 have previously been identified as a minimal peptide (KR-12) that retains antibacterial activity with decreased cytotoxicity. In this study, analogues of KR-12 were generated by Ala and Lys scans to identify key elements for activity. The improved analogues displayed no significant toxicity against against human cells.
study provides new insights into the fascinating plasticity of LL-37 demonstrated at atomic resolution and opens the venue for LL-37-based molecules as novel antibiotics.
LL-37 triggers release of nucleic acids from human mast cells but not the formation of extracellular trap-like structures.
LL-37 boosts the proliferation of unspecifically activated CD4(+) T cells via an increased calcium signalling independent of antigen-presenting cells
Human cathelicidin peptide LL-37 is significantly induced in the genital tracts of women diagnosed positive for Chlamydia trachomatis. Both the LL-37-stimulated IL-6/8 production in human endometrial epithelial cells and the LL-37-induced neutrophil chemotaxis are blocked by C. trachomatis plasmid-encoded Pgp3.
Serum cathelicidin level can be used as an early marker for the presence and progression of Diabetic nephropathy in T1 Diabetes mellitus patients.
Cultures of Escherichia coli with high cell density exhibit two distinct subpopulations: a non-growing population that absorb LL37 peptides and a growing population that survive owing to the sequestration of the antimicrobial peptides by others explaining the increase of the minimum inhibitory concentration with increasing cell density.
results indicate that PGE2 inhibits hCAP18/LL-37 expression, especially VD3-induced cathelicidin and autophagy, which may reduce host defense against Mtb. Accordingly, antagonists of EP4 may constitute a novel adjunctive therapy in Mtb infection.
The correlation between serum LL-37 and high-density lipoprotein cholesterol levels suggests that LL-37 may play a key role in regulation of cholesterol levels in hypercholesterolemia.
LL-37/CRAMP represents an important mediator of platelet activation and thrombo-inflammation.
Low vitamin D3 status and higher systemic levels of LL-37 may be a consequence of reduced TB control and enhanced pathological inflammation.
these data show that LL-37 affects surface and intracellular Toll-Like Receptor expression in tissue mast cells
This review describes novel advances involving the roles and mechanisms of human cathelicidin LL-37 in cancer.
this study shows that LL-37 serum level correlates with healing of venous leg ulcers
Elevated serum levels of LL-37 in bipolar patients may suggest the role of this peptide in the pathomechanism of BD.
LL-37 serum levels are not affected by body composition in elderly women with unipolar depression.
The findings support a role for STAT3 and HIF-1A in the regulation of LL-37 expression.
In silico docking study have confirmed the high binding affinities of multiple 9-mer peptides derived from LL-37 to the HLA-C*06:02 molecule proposed a mechanism of the interaction between this LL-37-HLA-C*06:02 complex and T cells via TCRs.
Injection of CAP18 into juvenile rainbow trout before exposure to Yersinia ruckeri was associated with lowered mortality compared to non-medicated fish although it was less effective than the conventional antibiotic oxolinic acid.
Pattern recognition receptors such as TLR5 may be involved in the stimulation of cathelicidin expression, and the signalling cascade can include PI3-kinase and cellular trafficking compartments.
Data show that the gene expression of asCATH1 (AAW55907, AY728057) and asCATH2 (AAT44537, AY360357) were upregulated in the gills and spleen during bacterial challenge from Y. ruckeri.
p15 proteins are stored in the specific (secondary) granules of rabbit neutrophils and are secreted extracellularly after inflammatory stimulation.
The p15 proteins exhibit antimicrobial synergy with another rabbit cathelicidin (CAP-18) and with the rabbit Bactericidal/permeability-increasing protein (BPI).
CRAMP is critical in maintaining colon microbiota balance.
Mice treated with BMMNCs pre-incubated with CRAMP had smaller scars, enhanced cardiac recovery and less adverse remodeling. Histologically, this group had higher capillary density. Similarly, sustained CRAMP release from hydrogels enhanced the therapeutic effect of SDF-1, leading to enhanced functional recovery
CRAMP deficiency impairs phagocytosis in cultured microglia cells after exposure to N. meningitides.
Immunoblotting, qPCR, ChIP and siRNA-mediated gene knockdown studies revealed that the activation of phosphatidylinositol 3-kinase/protein kinase C zeta pathways in poly(I:C)-stimulated cells underlies Sp1 phosphorylation and recruitment to the mCRAMP promoter, leading to enhanced transcription
The effect on insulin resistance found in Cramp-/- mice is solely due to leukocyte infiltration and not due to inflammatory phenotype of macrophages. Therefore we conclude that cathelicidin causes insulin resistance by the recruitment of myeloid cells into the adipose tissue.
Cathelicidin is required for innate resistance to M. tuberculosis in a relevant animal model and is a key mediator in regulation of the levels of pro-inflammatory cytokines by calcium and cyclic nucleotides.
Histological examination confirmed that CRAMP deficiency worsened the pancreatic inflammatory condition. These results indicate that CRAMP may be considered a novel modulatory mediator in mouse experimental AP.
promotes olfactory epithelium inflammation
overexpressed CRAMP in prostate tumor initially chemoattracts early myeloid progenitors to tumor microenvironment and mediates differentiation and polarization of early myeloid progenitors into protumorigenic M2 macrophages during PCa progression
critical role in prevention of RSV-mediated disease postinfection exogenously applied LL-37 is protective against RSV-mediated disease in vivo.
The aim of this project was to examine the functional impact of the human cathelicidin LL-37 and the mouse cathelicidin-related AMP (CRAMP) on the pathogenesis of lupus and arthritis.
Cathelicidin, expressed by immune cells in the tumor microenvironment, promotes colon cancer growth through activation of the PTEN/PI3K/Akt and Wnt/beta-catenin signaling pathways.
pancreatic beta-cells' production is controlled by short-chain fatty acids produced by the gut microbiota, and is defective in non-obese diabetic (NOD) mice
Data indicate the role of cathelicidin-related antimicrobial peptide (CRAMP) as part of the innate immune defense against pathogens in bacterial CNS infections.
Hypoxia-inducible factor-1alpha (HIF-1alpha), a transcription factor important for activating innate immune effectors, and the antimicrobial peptide LL-37 (CRAMP in mice) are key determinants of C. albicans colonization resistance.
Specific structural motifs in syndecan-1 HS promote Staphylococcus aureus corneal infection by inhibiting neutrophil CRAMP.
these findings show that the production of an antimicrobial peptide Camp by adipocytes is an important element for protection against S. aureus infection of the skin
Cathelicidin-deficient (Cnlp(-/-)) mice produce much less LTB4 and TXB2 in vivo in response to TNF-alpha compared with control mice.
observations indicate a nonredundant role for Fpr2 and its agonist CRAMP in DC maturation in immune responses.
Characterization of single nucleotide polymorphisms (SNPs) and insertion-deletion (indel) polymorphisms within the bovine CATHL gene family.
This gene encodes a member of an antimicrobial peptide family, characterized by a highly conserved N-terminal signal peptide containing a cathelin domain and a structurally variable cationic antimicrobial peptide, which is produced by extracellular proteolysis from the C-terminus. The encoded protein has several functions in addition to antimicrobial activity, including cell chemotaxis, immune mediator induction and inflammatory response regulation.
18 kDa cationic antimicrobial protein
, cathelicidin antimicrobial peptide
, cathelicidin-derived antimicrobial peptide 2
, 18 kDa cationic protein
, 18 kDa lipopolysaccharide-binding protein
, antimicrobial protein CAP18
, cathelin-like protein
, cathelin-related antimicrobial peptide
, cathelicidin 2
, myeloid antimicrobial peptide 27
, antimicrobial peptide
, antibacterial peptide BMAP-34
, cathelicidin 7
, neutrophil cationic antibacterial polypeptide of 11 kDa